1W6V

Solution structure of the DUSP domain of hUSP15

Summary for 1W6V

• Entry DOI: 10.2210/pdb1w6v/pdb
• Descriptor: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15 (1 entity in total)
• Functional Keywords: hydrolase, uch, usp, dub, deubiquitylation, deubiquitinating enzyme, ubiquitin, ubiquitin specific protease, ubiquitin carboxyterminal hydrolase, cleavage, usp15, dub15, ubp15, endopeptidase, thiolesterase, dusp, structural proteomics in europe, spine, structural genomics
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 16149.08

Authors

De Jong, R.D.,Ab, E.,Diercks, T.,Truffault, V.,Daniels, M.,Kaptein, R.,Folkers, G.E. (deposition date: 2004-08-24, release date: 2006-01-12, Last modification date: 2024-05-15)

Primary citation

De Jong, R.N.,Ab, E.,Diercks, T.,Truffault, V.,Daniels, M.,Kaptein, R.,Folkers, G.E.
Solution Structure of the Human Ubiquitin-Specific Protease 15 Dusp Domain.
J.Biol.Chem., 281:5026-, 2006

PubMed Abstract: Ubiquitin-specific proteases (USPs) can remove covalently attached ubiquitin moieties from target proteins and regulate both the stability and ubiquitin-signaling state of their substrates. All USPs contain a conserved catalytic domain surrounded by one or more subdomains, some of which contribute to target recognition. One such specific subdomain, the DUSP domain (domain present in ubiquitin-specific proteases), is present in at least seven different human USPs that regulate the stability of or interact with the hypoxia-inducible transcription factor HIF1-alpha, the Von Hippel-Lindau protein (pVHL), cullin E3 ligases, and BRCA2. We describe the NMR solution structure of the DUSP domain of human USP15, recently implicated in COP9 (constitutive photomorphogenic gene 9)-signalosome regulation. Its tripod-like structure consists of a 3-fold alpha-helical bundle supporting a triple-stranded anti-parallel beta-sheet. The DUSP domain displays a novel fold, an alpha/beta tripod (AB3). DUSP domain surface properties and previously described work suggest a potential role in protein/protein interaction or substrate recognition.

PubMed: 16298993
DOI: 10.1074/JBC.M510993200

Experimental method

SOLUTION NMR